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Conserved domains on  [gi|2118836884|gb|UDE30233|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Ceriodaphnia megops]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-200 1.70e-134

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 386.15  E-value: 1.70e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00153   31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00153  111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00153  191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 1.70e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 386.15  E-value: 1.70e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00153   31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00153  111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00153  191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 1.79e-119

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 347.16  E-value: 1.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:cd01663    24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:cd01663   104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:cd01663   184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 5.88e-70

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 5.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:COG0843   195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-200 7.64e-42

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 145.79  E-value: 7.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAvesGAGTGWTVYPPLSAgiahagasVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLdRIPLFAWAVGITA 160
Cdd:pfam00115  99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNtsffdpAGGGDPILYQ 200
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-200 1.70e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 386.15  E-value: 1.70e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00153   31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00153  111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00153  191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 230
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-200 1.79e-119

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 347.16  E-value: 1.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:cd01663    24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:cd01663   104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:cd01663   184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 223
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-200 8.89e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 336.26  E-value: 8.89e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00167   33 LSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00167  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTT 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00167  193 ILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-200 1.39e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 330.40  E-value: 1.39e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00223   30 LSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00223  110 LSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTA 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00223  190 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 229
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-200 6.73e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 328.61  E-value: 6.73e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00142   31 LSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00142  111 LSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITA 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00142  191 ILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ 230
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-200 4.44e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 324.35  E-value: 4.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00116   33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00116  113 LASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00116  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-200 4.95e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 301.05  E-value: 4.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00007   30 MSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00007  110 VSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITV 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00007  190 VLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 229
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-200 1.22e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 297.51  E-value: 1.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00037   33 MSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00037  113 LASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00037  193 FLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQ 232
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-200 7.57e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 295.64  E-value: 7.57e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00103   33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00103  113 LASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00103  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-200 7.99e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 295.68  E-value: 7.99e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00183   33 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00183  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00183  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ 232
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-200 2.33e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 294.16  E-value: 2.33e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00077   33 LSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00077  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00077  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQ 232
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-200 1.29e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 282.10  E-value: 1.29e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00184   35 FSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00184  115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTT 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00184  195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 234
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-200 8.48e-93

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 280.55  E-value: 8.48e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00182   35 FSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00182  115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITA 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00182  195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQ 234
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-200 8.92e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 274.64  E-value: 8.92e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00079   34 LSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAgIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00079  114 LDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTV 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00079  193 FLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQ 232
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-200 9.12e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 259.95  E-value: 9.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00026   34 FSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:MTH00026  114 LGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITA 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00026  194 ILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQ 233
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-200 6.93e-76

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 235.12  E-value: 6.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPlMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:cd00919    22 LALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:cd00919   101 LSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTA 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:cd00919   181 ILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQ 220
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-200 5.88e-70

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 221.54  E-value: 5.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:COG0843   195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQ 234
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-200 8.69e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 192.20  E-value: 8.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:MTH00048   34 LSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGgaVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLdRIPLFAWAVGITA 160
Cdd:MTH00048  114 LLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTS 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:MTH00048  191 ILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQ 230
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-200 7.53e-58

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 189.33  E-value: 7.53e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:cd01662    28 DALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAVESGAGTGWTVYPPLSAGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITA 160
Cdd:cd01662   107 NASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTS 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNTSFFDPAGGGDPILYQ 200
Cdd:cd01662   187 ILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQ 226
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-200 7.64e-42

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 145.79  E-value: 7.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884   1 LSMLIRVELGQSGSLIGDDQIYNVIVTAHAFIMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  81 LVGGAvesGAGTGWTVYPPLSAgiahagasVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLdRIPLFAWAVGITA 160
Cdd:pfam00115  99 LASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2118836884 161 LLLLLSLPVFAGAITMLLTDRNLNtsffdpAGGGDPILYQ 200
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQ 200
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 22-199 5.41e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 138.53  E-value: 5.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884  22 YNVIVTAHAFIMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPRLNNLSFWLLPPSLTLLLVGGAVESGAGTGWTVYPPLS 101
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118836884 102 AGIAHAGASVDLSIFSLHLAGISSILGAINFITTIINMRSQGMTLDRIPLFAWAVGITALLLLLSLPVFAGAITMLLTDR 181
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170
                  ....*....|....*...
gi 2118836884 182 NLNTSFFDPAGGGDPILY 199
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMY 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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